7xpv: Difference between revisions

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'''Unreleased structure'''


The entry 7xpv is ON HOLD  until Paper Publication
==crysteal structure of MtdL-S228A-His soaked with GDP-Fucf and Mn==
<StructureSection load='7xpv' size='340' side='right'caption='[[7xpv]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7xpv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinactinospora_thermotolerans Marinactinospora thermotolerans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XPV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GRJ:[[(2~{R},3~{S},4~{R},5~{R})-5-(2-azanyl-6-oxidanyl-purin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]+[(2~{S},3~{S},4~{S},5~{R})-3,4-bis(oxidanyl)-5-[(1~{S})-1-oxidanylethyl]oxolan-2-yl]+hydrogen+phosphate'>GRJ</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7xpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xpv OCA], [https://pdbe.org/7xpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xpv RCSB], [https://www.ebi.ac.uk/pdbsum/7xpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xpv ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Members of glycosyltransferase family 75 (GT75) not only reversibly catalyze the autoglycosylation of a conserved arginine residue with specific NDP-sugars but also exhibit NDP-pyranose mutase activity that reversibly converts specific NDP-pyranose to NDP-furanose. The latter activity provides valuable NDP-furanosyl donors for glycosyltransferases and requires a divalent cation as a cofactor instead of FAD used by UDP-D-galactopyranose mutase. However, details of the mechanism for NDP-pyranose mutase activity are not clear. Here we report the first crystal structures of GT75 family NDP-pyranose mutases. The novel structures of GT75 member MtdL in complex with Mn(2+) and GDP, GDP-D-glucopyranose, GDP-L-fucopyranose, GDP-L-fucofuranose, respectively, combined with site-directed mutagenesis studies, reveal key residues involved in Mn(2+) coordination, substrate binding, and catalytic reactions. We also provide a possible catalytic mechanism for this unique type of NDP-pyranose mutase. Taken together, our results highlight key elements of an enzyme family important for furanose biosynthesis.


Authors:  
Structures of the NDP-pyranose mutase belonging to glycosyltransferase family 75 reveal residues important for Mn(2+) coordination and substrate binding.,Du X, Chu X, Liu N, Jia X, Peng H, Xiao Y, Liu L, Yu H, Li F, He C J Biol Chem. 2023 Feb;299(2):102903. doi: 10.1016/j.jbc.2023.102903. Epub 2023 , Jan 13. PMID:36642179<ref>PMID:36642179</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 7xpv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Marinactinospora thermotolerans]]
[[Category: He C]]
[[Category: Li FD]]

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